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Literature summary for 3.3.2.6 extracted from

  • Rudberg, P.C.; Tholander, F.; Thunnissen, M.M.; Samuelsson, B.; Haeggstrom, J.Z.
    Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375 (2002), Proc. Natl. Acad. Sci. USA, 99, 4215-4220.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine the enzyme catalyses the hydrolysis of leukotriene A4 into the proinflammatory substance leukotriene B4 Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant enzymes expressed in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type enzyme and mutant D375N Homo sapiens

Protein Variants

Protein Variants Comment Organism
D368N epoxide hydrolase activity: 72% of Km of wild type enzyme, aminopeptidase activity: 107% of Km of wild type enzyme Homo sapiens
D371N epoxide hydrolase activity: 51% of Km of wild type enzyme, aminopeptidase activity: 77% of Km of wild type enzyme Homo sapiens
D373N epoxide hydrolase activity: 43% of Km of wild type enzyme, aminopeptidase activity: 101% of Km of wild type enzyme Homo sapiens
D375A near-complete loss of the epoxide hydrolase activity, aminopeptidase activity exhibits unsaturable enzyme kinetic Homo sapiens
D375E complete loss of the epoxide hydrolase activity, aminopeptidase activity: 152% of Km of wild type enzyme Homo sapiens
D375N complete loss of the epoxide hydrolase activity, aminopeptidase activity exhibits unsaturable enzyme kinetic Homo sapiens
H139Q epoxide hydrolase activity: 167% of Km of wild type enzyme, aminopeptidase activity: 359% of Km of wild type enzyme Homo sapiens
Q134A epoxide hydrolase activity exhibits unsaturable enzyme kinetics within the range observed, aminopeptidase activity: 157% of Km of wild type enzyme Homo sapiens
Q134L significantly increased epoxide hydrolase activity, aminopeptidase activity: 87% of Km of wild type enzyme Homo sapiens
Q134N epoxide hydrolase activity: 148% of Km of wild type enzyme, aminopeptidase activity: 108% of Km of wild type enzyme Homo sapiens
Y267F epoxide hydrolase activity: 58% of Km of wild type enzyme, aminopeptidase activity: 64% of Km of wild type enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006 0.028 leukotriene A4 pH 8.0, wild-type enzyme in comparison to mutant enzymes Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
leukotriene A4 + H2O Homo sapiens biosynthesis of leukotriene B4 leukotriene B4
-
?

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
-
-
-
Drosophila melanogaster
-
-
-
Homo sapiens P09960
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-
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
leukotriene A4 + H2O = leukotriene B4 Asp375 acts as a critical determinant for the stereoselective introduction of the 12R-hydroxyl group, possibly assisted by Gln134 and thus the biological activity of leukotriene B4 Homo sapiens
leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase Saccharomyces cerevisiae
leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
leukotriene A4 + H2O
-
Homo sapiens leukotriene B4
-
?
leukotriene A4 + H2O biosynthesis of leukotriene B4 Homo sapiens leukotriene B4
-
?
additional information
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Saccharomyces cerevisiae ?
-
?
additional information
-
Caenorhabditis elegans ?
-
?
additional information
-
Homo sapiens ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.21 0.47 leukotriene A4 pH 8.0, wild-type enzyme in comparison to mutant enzymes Homo sapiens